|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
41-517 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 990.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 41 EKSRSSWIKQLNASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDM 120
Cdd:PLN03226 1 EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 121 AETLCQKRALEAFQLDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMP 200
Cdd:PLN03226 81 IETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 201 YRLDENTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVV 280
Cdd:PLN03226 161 YRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 281 TTTTHKSLRGPRGAMIFFRKGLKEINKQGKEVMYDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVL 360
Cdd:PLN03226 241 TTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 361 RNCSKFAETLLAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRG 440
Cdd:PLN03226 321 ANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734095 441 FIEEDFAKVAEYFDLAVKIALKIKAESqGTKLKDFVATMQSNEKlQSEMSKLREMVEEYAKQFPTIGFEKETMRYKE 517
Cdd:PLN03226 401 LVEKDFEKVAEFLHRAVTIALKIQKEH-GKKLKDFKKGLESNDF-SKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
55-452 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 760.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 55 LDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFQ 134
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 135 LDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDENTGYIDYDQ 214
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 215 LEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGPRGA 294
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 295 MIFFRKGLKEINKQGKEVMYDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKG 374
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734095 375 YDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFIEEDFAKVAEY 452
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
57-479 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 638.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 57 EIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFQLD 136
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 137 pskwGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTdtkKISAVSIFFETMPYRLDENTGYIDYDQLE 216
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 217 KSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGPRGAMI 296
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 297 FFRKGlkeinkqgkevmyDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKGYD 376
Cdd:cd00378 235 LTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 377 LVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVS-AMVPGGIRMGTPALTSRGFIEEDFAKVAEYFDL 455
Cdd:cd00378 302 VVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIAR 381
|
410 420
....*....|....*....|....
gi 1063734095 456 AVKIALKIKAESqgtKLKDFVATM 479
Cdd:cd00378 382 ALKDAEDVAVAE---EVRKEVAEL 402
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
52-504 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 585.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 52 NASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 131
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 132 AFQldpSKWgVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDENTGYID 211
Cdd:COG0112 82 LFG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 212 YDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGP 291
Cdd:COG0112 153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 292 RGAMIFFRKglkeinkqgkevmyDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLL 371
Cdd:COG0112 233 RGGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 372 AKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFIEEDFAKVA 450
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1063734095 451 EYFDLAVKialkikaesqgtklkdfvatmqsNEKLQSEMSKLREMVEEYAKQFP 504
Cdd:COG0112 379 ELIADVLD-----------------------NPEDEAVLAEVREEVKELCKRFP 409
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
41-517 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 990.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 41 EKSRSSWIKQLNASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDM 120
Cdd:PLN03226 1 EKSMVSVPKWGNAPLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 121 AETLCQKRALEAFQLDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMP 200
Cdd:PLN03226 81 IETLCQKRALEAFRLDPEKWGVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTDGKKISATSIYFESMP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 201 YRLDENTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVV 280
Cdd:PLN03226 161 YRLDESTGLIDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 281 TTTTHKSLRGPRGAMIFFRKGLKEINKQGKEVMYDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVL 360
Cdd:PLN03226 241 TTTTHKSLRGPRGGMIFFRKGPKPPKGQGEGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 361 RNCSKFAETLLAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRG 440
Cdd:PLN03226 321 ANAAALANRLMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDSSALVPGGVRIGTPAMTSRG 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063734095 441 FIEEDFAKVAEYFDLAVKIALKIKAESqGTKLKDFVATMQSNEKlQSEMSKLREMVEEYAKQFPTIGFEKETMRYKE 517
Cdd:PLN03226 401 LVEKDFEKVAEFLHRAVTIALKIQKEH-GKKLKDFKKGLESNDF-SKDIEALRAEVEEFATSFPMPGFDKESMKYKE 475
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
51-508 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 776.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 51 LNASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRAL 130
Cdd:PTZ00094 11 LNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 131 EAFQLDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDENtGYI 210
Cdd:PTZ00094 91 EAFGLDPEEWGVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFYTAKKKVSATSIYFESLPYQVNEK-GLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 211 DYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRG 290
Cdd:PTZ00094 170 DYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 291 PRGAMIFFRKGLKEinkqgkevmyDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETL 370
Cdd:PTZ00094 250 PRSGLIFYRKKVKP----------DIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 371 LAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFIEEDFAKVA 450
Cdd:PTZ00094 320 EKRGYDLVTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSALNPSGVRLGTPALTTRGAKEKDFKFVA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734095 451 EYFDLAVKIALKIKaESQGTKLKDFVATMQSNEKLQsemsKLREMVEEYAKQFPTIGF 508
Cdd:PTZ00094 400 DFLDRAVKLAQEIQ-KQVGKKLVDFKKALEKNPELQ----KLRQEVVEFASQFPFPGI 452
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
55-452 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 760.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 55 LDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFQ 134
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 135 LDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDENTGYIDYDQ 214
Cdd:pfam00464 81 LDPAKWGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 215 LEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGPRGA 294
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 295 MIFFRKGLKEINKQGKEVMYDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKG 374
Cdd:pfam00464 241 MIFYRKGVKSVDKTGKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063734095 375 YDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFIEEDFAKVAEY 452
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGDKSAFVPSGLRLGTPALTSRGFGEADFEKVAGF 398
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
57-479 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 638.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 57 EIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFQLD 136
Cdd:cd00378 2 DVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 137 pskwGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTdtkKISAVSIFFETMPYRLDENTGYIDYDQLE 216
Cdd:cd00378 82 ----YANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFT---KVSASGKLFESVPYGVDPETGLIDYDALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 217 KSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGPRGAMI 296
Cdd:cd00378 155 KMALEFKPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 297 FFRKGlkeinkqgkevmyDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKGYD 376
Cdd:cd00378 235 LTRKG-------------ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 377 LVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVS-AMVPGGIRMGTPALTSRGFIEEDFAKVAEYFDL 455
Cdd:cd00378 302 VVSGGTDNHLVLVDLRPKGITGKAAEDALEEAGITVNKNTLPWDPSsPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIAR 381
|
410 420
....*....|....*....|....
gi 1063734095 456 AVKIALKIKAESqgtKLKDFVATM 479
Cdd:cd00378 382 ALKDAEDVAVAE---EVRKEVAEL 402
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
52-504 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 585.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 52 NASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 131
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 132 AFQldpSKWgVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDENTGYID 211
Cdd:COG0112 82 LFG---AEH-ANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKGYNVVSYGVDPETGLID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 212 YDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGP 291
Cdd:COG0112 153 YDEVRKLALEHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 292 RGAMIFFRKglkeinkqgkevmyDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLL 371
Cdd:COG0112 233 RGGLILCNE--------------ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 372 AKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFIEEDFAKVA 450
Cdd:COG0112 299 ERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEKALERAGITVNKNAIPFDPrSPFVTSGIRIGTPAVTTRGMKEAEMEEIA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1063734095 451 EYFDLAVKialkikaesqgtklkdfvatmqsNEKLQSEMSKLREMVEEYAKQFP 504
Cdd:COG0112 379 ELIADVLD-----------------------NPEDEAVLAEVREEVKELCKRFP 409
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
30-509 |
0e+00 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 584.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 30 SSLSTAAMAESEKSRSSWIKQL-NASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPG 108
Cdd:PLN02271 103 SSSKRAAVDSGLESRRAAVRAWgNQPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 109 ARYYGGNEYIDMAETLCQKRALEAFQLDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDT-K 187
Cdd:PLN02271 183 ARYYTGNQYIDQIERLCCERALAAFGLDSEKWGVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYYTPGgK 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 188 KISAVSIFFETMPYRLDENTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAA 267
Cdd:PLN02271 263 KVSGASIFFESLPYKVNPQTGYIDYDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 268 GVIPSPFEYADVVTTTTHKSLRGPRGAMIFFRKGLKeINKQGKEV-------MYDYEDRINQAVFPGLQGGPHNHTITGL 340
Cdd:PLN02271 343 KECVNPFDYCDIVTSTTHKSLRGPRGGIIFYRKGPK-LRKQGMLLshgddnsHYDFEEKINFAVFPSLQGGPHNNHIAAL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 341 AVALKQARTPEYKAYQDQVLRNCSKFAETLLAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGD 420
Cdd:PLN02271 422 AIALKQVATPEYKAYMQQVKKNAQALASALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGD 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 421 VSAMVPGGIRMGTPALTSRGFIEEDFAKVAEYFDLAVKIALKIKAEsQGTKLKDFVATMQSNEklqsEMSKLREMVEEYA 500
Cdd:PLN02271 502 NGTISPGGVRIGTPAMTSRGCLESDFETIADFLLRAAQIASAVQRE-HGKLQKEFLKGLQNNK----DIVELRNRVEAFA 576
|
....*....
gi 1063734095 501 KQFPTIGFE 509
Cdd:PLN02271 577 SQFAMPGFD 585
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
50-508 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 569.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 50 QLNASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRA 129
Cdd:PRK00011 1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 130 LEAFQldpSKWgVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDENTGY 209
Cdd:PRK00011 81 KELFG---AEY-ANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHG-----SPVNFSGKLYNVVSYGVDEETGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 210 IDYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLR 289
Cdd:PRK00011 152 IDYDEVEKLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 290 GPRGAMIFFRKglKEINKQgkevmydyedrINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAET 369
Cdd:PRK00011 232 GPRGGLILTND--EELAKK-----------INSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 370 LLAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFIEEDFAK 448
Cdd:PRK00011 299 LAERGFRVVSGGTDNHLVLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPrSPFVTSGIRIGTPAITTRGFKEAEMKE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 449 VAEYFDLAVKialkikaesqgtklkdfvatmqsNEKLQSEMSKLREMVEEYAKQFPTIGF 508
Cdd:PRK00011 379 IAELIADVLD-----------------------NPDDEAVIEEVKEEVKELCKRFPLYKY 415
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
52-452 |
1.69e-172 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 492.55 E-value: 1.69e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 52 NASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALE 131
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 132 AFQLDpskwGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGyqtdtKKISAVSIFFETMPYRLDENTGYID 211
Cdd:PRK13034 86 LFGCD----YANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHG-----AKVSLSGKWYNAVQYGVDRLTGLID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 212 YDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGP 291
Cdd:PRK13034 157 YDEVEELAKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 292 RGAMIFFRKglKEINKqgkevmydyedRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLL 371
Cdd:PRK13034 237 RGGMILTND--EEIAK-----------KINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 372 AKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDV-SAMVPGGIRMGTPALTSRGFIEEDFAKVA 450
Cdd:PRK13034 304 ERGYDLVSGGTDNHLLLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTeSPFVTSGIRIGTPAGTTRGFGEAEFREIA 383
|
..
gi 1063734095 451 EY 452
Cdd:PRK13034 384 NW 385
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
29-451 |
8.55e-110 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 335.47 E-value: 8.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 29 MSSLSTAAMAESEKSRSSWIKQLNASLDEI---DPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEG 105
Cdd:PRK13580 1 SLLDKALLNASGKDQQNLASTAYLAALDVIlhvEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 106 YPGARYYGGNEYIDMAETLCQKRALEAFQLDPSKwgvnVQSLSGSPANFQVYTALLKPH--------------------- 164
Cdd:PRK13580 81 TPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY----VQPHSGADANLVAFWAILAHKvespaleklgaktvndlteed 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 165 ----------ERIMALDLPHGGHLSHGYQTDtkkISavSIFFETMPYRLDENTGYIDYDQLEKSAVLFRPKLIVAGASAY 234
Cdd:PRK13580 157 wealraelgnQRLLGMSLDSGGHLTHGFRPN---IS--GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 235 ARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIP---SPFEYADVVTTTTHKSLRGPRGAMIFFRKglkeinkqgke 311
Cdd:PRK13580 232 PRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHADIVTTTTHKTLRGPRGGLVLAKK----------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 312 vmyDYEDRINQAVfPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKGYDLVSGGTDNHLVLVNL 391
Cdd:PRK13580 301 ---EYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGFLKRGARLVTGGTDNHLVLIDV 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063734095 392 KNKGIDGSRVEKVLELVHIAANKNTVPGDVS-AMVPGGIRMGTPALTSRGFIEEDFAKVAE 451
Cdd:PRK13580 377 TSFGLTGRQAESALLDAGIVTNRNSIPSDPNgAWYTSGIRLGTPALTTLGMGSDEMDEVAE 437
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
122-299 |
4.22e-30 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 115.56 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 122 ETLCQKRALEAFQldPSKWGVNVQSlSGSPANFQVYTALLKPHERIMALDLPHGGHLSHgyqtdtkkiSAVSIFFETMPY 201
Cdd:cd01494 2 LEELEEKLARLLQ--PGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV---------AAELAGAKPVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 202 RLDENTGY-IDYDQLEKSAVLFRPKLIVAGASAYAR--LYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYAD 278
Cdd:cd01494 70 PVDDAGYGgLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGAD 149
|
170 180
....*....|....*....|.
gi 1063734095 279 VVTTTTHKSLRGPRGAMIFFR 299
Cdd:cd01494 150 VVTFSLHKNLGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
142-284 |
2.25e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 40.37 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 142 VNVQSLSGSPANFQVYTALLKPHERIMALDLPhgGHLSHgyqtdtkKISAVSIFFETMPYRL-DENTGYIDYDQLEKsAV 220
Cdd:pfam00155 64 AAVVFGSGAGANIEALIFLLANPGDAILVPAP--TYASY-------IRIARLAGGEVVRYPLyDSNDFHLDFDALEA-AL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063734095 221 LFRPKLIV-AGAS----AYARLYDYARIRKVCNKQKAVMLADMAHI----SGLVAAGVIPSPFEYADVVTTTT 284
Cdd:pfam00155 134 KEKPKVVLhTSPHnptgTVATLEELEKLLDLAKEHNILLLVDEAYAgfvfGSPDAVATRALLAEGPNLLVVGS 206
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
200-451 |
6.98e-03 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 38.86 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 200 PYRLDENTGYIDYDQLEKSAVLFRPKLIV-------AGasayaRLYDYARIRKV---CNKQKAVMLADMAHiSGLVAAGV 269
Cdd:cd00609 109 PVPLDEEGGFLLDLELLEAAKTPKTKLLYlnnpnnpTG-----AVLSEEELEELaelAKKHGILIISDEAY-AELVYDGE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 270 IPSPFEYAD-----VVTTTTHKSLRGP--RGAMIFFRKglkeinkqgKEVMYDYEDRInqavfPGLQGGPHNHTITGLAV 342
Cdd:cd00609 183 PPPALALLDayervIVLRSFSKTFGLPglRIGYLIAPP---------EELLERLKKLL-----PYTTSGPSTLSQAAAAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063734095 343 ALKQaRTPEYKAYQDQVLRNCSKFAETLLAKGYDLVSGGTDNHLVLVNLkNKGIDGSRVEKVLELVHIAAnknTVPGDVS 422
Cdd:cd00609 249 ALDD-GEEHLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVV---RPGSAFG 323
|
250 260
....*....|....*....|....*....
gi 1063734095 423 AMVPGGIRMGTpaltsrGFIEEDFAKVAE 451
Cdd:cd00609 324 EGGEGFVRLSF------ATPEEELEEALE 346
|
|
| |
